Oligomeric Structure of the MALT1 Tandem Ig-Like Domains CARD and Tandem Ig Domains of MALT1
2011
Understanding MALT1 Protein Structure and Function
publication
Evidence: moderate
Author Information
Author(s): Qiu Liyan, Dhe-Paganon Sirano
Primary Institution: Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada
Hypothesis
How does the MALT1 protein oligomerize to activate the NF-κB signaling pathway?
Conclusion
The study reveals that MALT1 can form oligomers, which may play a crucial role in its function in the immune response.
Supporting Evidence
- MALT1 plays an important role in the adaptive immune program.
- The tandem Ig-like domains of MALT1 exist as a mixture of dimer and tetramer in solution.
- High-resolution structures reveal a protein-protein interface that stabilizes MALT1 oligomerization.
Takeaway
MALT1 is a protein that helps our immune system work, and it can stick together in groups to do its job better.
Methodology
The study used structural biology techniques, including crystallization and size-exclusion chromatography, to analyze the MALT1 protein.
Digital Object Identifier (DOI)
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